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Escolher formato: Padrão Ficha Formato Reduzido Nomes MARC Campos MARC
No. Registro   001265304
Tipo de material   ARTIGO DE PERIODICO - INTERNACIONAL
Cód. publicação   Link10.1016/s0006-2952(02)01210-8 DOI
Entrada Principal   LinkAndrião-Escarso, Sílvia Helena (**)
Título   LinkStructural and functional characterization of an acidic platelet aggregation inhibitor and hypotensive phospholipase ’A IND.2’ from Bothrops jararacussu snake venom.
Imprenta   New York, 2002.
Descrição   p. 723-732.
Idioma   Inglês
Assunto   LinkBIOQUÍMICA
  LinkFARMACOLOGIA
  LinkVENENOS DE ORIGEM ANIMAL
Autor Secundário   LinkSoares, Andreimar Martins (*)
  LinkFontes, Marcos Roberto de Mattos (*) NAC Depto. de Física e Biofísica, IB, Universidade Estadual Paulista, Botucatu-SP
  LinkFuly, André L. (*) NAC Departamento de Bioquímica Médica, Centro de Ciências da Saúde, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ
  LinkCorrêa, Fernando Morgan de Aguiar
  LinkRosa, José C. (*)
  LinkGreene, Lewis Joel
  LinkGiglio, José Roberto (*)
Fonte   LinkIn: Biochemical Pharmacology, New York, v. 64, p. 723-732, 2002, ISSN: 0006-2952
Localiz.Eletrônica   e-mail do autor -- mailto://jrgiglio@fmrp.usp.br
Localiz.Eletrônica    Acesso para publicação em formato eletrônico 
Resumo/Outros   An acidic (pI’DA ORDEM DE’4.5) phospholipase ’A IND. 2’ (BthA-I-PL’A IND.2’) was isolated from Bothrops jararacussu snake venom by ion-exchange chromatography on a CM-Sepharose column followed by reverse phase chromatography on an RP-HPLC C-18 column. It is an ’DA ORDEM DE’13.7 kDa single chain Asp49 PL’A IND.2’ with approximately 122 amino acid residues, 7 disulfide bridges, and the following N-terminal sequence: ’ANTPOT.1 SLWQFGKMINYVM-GESGVLQYLSYGCYCGLGGQGQPTDATDRCCFVHDCC’ POT.51’. Crystals of this acidic protein diffracted beyond 2.0 ’ângstron’ resolution. These crystals are monoclinic and have unit cell dimensions of a=33.9, b=63.8, c=49.1 ’ângstron’, and ’beta’=104.0’GRAUS’. Although not myotoxic, cytotoxic, or lethal, the protein was catalytically 3-4 times more active than BthTX-II, a basic D49 myotoxic PL’A IND.2’ from the same venom and other Bothrops venoms. Although it showed no toxic activity, it was able to induce time-independent edema, this activity being inhibited by EDTA. In addition, BthA-I-PL’A IND.2’ caused a hypotensive response in the rat and inhibited platelet aggregation. Catalytic, antiplatelet and other activities were abolished by chemical modification with 4-bromophenacyl bromide, which is known to covalently bind to His48 of the catalytic site. Antibodies raised against crude B. jararacussu venom recognized this acidic PL’A IND.2’, while anti-Asp49-BthTX-II recognized it weakly and anti-Lys49-BthTX-I showed the least
  cross-reaction. These data confirm that myotoxicity does not necessarily correlate with catalytic activity in native PL’A IND.2’ homologues and that either of these two activities may exist alone. BthA-I-PLA2, in addition to representing a relevant molecular model of catalytic activity, is also a promising hypotensive agent and platelet aggregation inhibitor for further studies
 
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Itens na Biblioteca   BCRP-Fac Medicina Rib PretoLibrary Info
Unidade USP   FMRP -- FAC DE MEDICINA DE RIBEIRÃO PRETO
  FMRP -- FAC DE MEDICINA DE RIBEIRÃO PRETO
  FMRP -- FAC DE MEDICINA DE RIBEIRÃO PRETO
  FMRP -- FAC DE MEDICINA DE RIBEIRÃO PRETO
  FMRP -- FAC DE MEDICINA DE RIBEIRÃO PRETO

Escolher formato: Padrão Ficha Formato Reduzido Nomes MARC Campos MARC


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